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EMSAs of wild-type and S326C OGG1

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posted on 2011-12-30, 17:52 authored by Jeff W. Hill, Michele K. Evans

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Taken from "Dimerization and opposite base-dependent catalytic impairment of polymorphic S326C OGG1 glycosylase"

Nucleic Acids Research 2006;34(5):1620-1632.

Published online 20 Mar 2006

PMCID:PMC1405821.

© The Author 2006. Published by Oxford University Press. All rights reserved

DNA damage binding affinities of wild-type and S326C OGG1 were measured by incubation with DNA substrates containing 8-oxoG·C (), 8-oxoG·T (), 8-oxoG·G (), 8-oxoG·A () and AP·C (). () Identical to the experiment in (A), with the addition of 1 mM DTT. Gel shifts of glycosylases were performed as described in Materials and Methods. In all panels, lane 1, no enzyme; lane 2, wild-type OGG1; lane 3, S326C OGG1.

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